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6F4N

Human JMJD5 in complex with MN and 2OG.

Summary for 6F4N
Entry DOI10.2210/pdb6f4n/pdb
Related6F4M 6F4O 6F4P 6F4Q 6F4R 6F4S 6F4T
DescriptorJmjC domain-containing protein 5, MANGANESE (II) ION, 2-OXOGLUTARIC ACID, ... (4 entities in total)
Functional Keywordsoxidoreductase, non-heme, iron, 2-oxoglutarate, dioxygenase, jmjc, jmjc domain, lysine-specific demethylase 8, jmjc domain-containing protein 5, arginyl c-3 hydroxylase, jmjd5, kdm8, oxygenase, hypoxia, dna-binding, metal-binding, translation, dsbh, facial triad, cytoplasm, jmjc hydroxylase, jmjc demethylase, kdms, post-translational modifications, ptm, beta-hydroxylation, hydroxylation, arginine hydroxylation, rcc1 domain-containing protein 1, rccd1, regulator of chromosome condensation, 40s ribosomal protein s6, rps6, ribosome biogenesis, transcription, epigenetic regulation, signaling, development, cell structure, transcription activator/inhibitor, phosphorylation, cancer, polymorphism
Biological sourceHomo sapiens (Human)
Cellular locationNucleus : Q8N371
Total number of polymer chains2
Total formula weight63119.24
Authors
Chowdhury, R.,Islam, M.S.,Schofield, C.J. (deposition date: 2017-11-29, release date: 2018-04-04, Last modification date: 2024-01-17)
Primary citationWilkins, S.E.,Islam, S.,Gannon, J.M.,Markolovic, S.,Hopkinson, R.J.,Ge, W.,Schofield, C.J.,Chowdhury, R.
JMJD5 is a human arginyl C-3 hydroxylase.
Nat Commun, 9:1180-1180, 2018
Cited by
PubMed: 29563586
DOI: 10.1038/s41467-018-03410-w
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.541 Å)
Structure validation

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